STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
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Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Afer_0100PFAM: Alpha/beta hydrolase fold-3 domain protein; KEGG: acr:Acry_0942 alpha/beta hydrolase domain- containing protein. (335 aa)    
Predicted Functional Partners:
nuoI
NADH-quinone oxidoreductase, chain I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
  
 
 0.834
Afer_0369
NADH-quinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family.
    
 
 0.812
Afer_0367
TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: msm:MSMEG_2059 NADH-quinone oxidoreductase chain E.
    
   0.800
Afer_1826
PFAM: Rieske [2Fe-2S] domain protein; KEGG: fal:FRAAL5110 ubiquinol-cytochrome c reductase iron-sulfur subunit (Rieske iron-sulfur protein).
   
   0.797
Afer_1377
PFAM: ferredoxin; Oxidoreductase FAD-binding domain protein; oxidoreductase FAD/NAD(P)-binding domain protein; KEGG: dar:Daro_0368 ferredoxin:oxidoreductase FAD/NAD(P)-binding:oxidoreductase FAD-binding region.
    
 
 0.777
acpP
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.
   
 
 0.761
acpP-2
Phosphopantetheine-binding; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family.
   
 
 0.761
nuoB
NADH-quinone oxidoreductase, B subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
    
   0.760
Afer_0368
PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: mxa:MXAN_1085 NADH dehydrogenase I, F subunit.
    
   0.747
Afer_0998
PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: sco:SCP1.160c putative oxidoreductase.
    
   0.747
Your Current Organism:
Acidimicrobium ferrooxidans
NCBI taxonomy Id: 525909
Other names: A. ferrooxidans DSM 10331, Acidimicrobium ferrooxidans DSM 10331, Acidimicrobium ferrooxidans ICP, Acidimicrobium ferrooxidans str. DSM 10331, Acidimicrobium ferrooxidans strain DSM 10331
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